Effect of calcium addition on the thermal denaturation of bovine apo-α-lactalbumin - a preliminary study.
作者： S. Dima , G. Râpeanu , N. Stănciuc
DOI:
关键词: Tryptophan 、 Quenching (fluorescence) 、 Crystallography 、 Chemistry 、 Molten globule 、 Lactalbumin 、 Calcium 、 Alpha-lactalbumin 、 Fluorescence spectroscopy 、 Denaturation (biochemistry)
摘要: Bovine �± -lactalbumin is known to be present in molten globule form its apo -state (i.e., Ca 2+ depleted state). In this preliminary study, heat -induced conformational changes were analyzed using the fluorescence spectroscopy at very low pH absence and presence of calcium ions. T he treatment caused decrease intrinsic , evidencing increase intramolecular quenching tryptophans. The two classes tryptophan residues (exposed buried) was reflected also Stern �Volmer plot, theKSVvalues used for estimating exposed tryptoph an protein.
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